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Avin C. Snyder
Researcher at University of Pittsburgh
Publications - 3
Citations - 455
Avin C. Snyder is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Endoplasmic-reticulum-associated protein degradation & Ubiquitin ligase. The author has an hindex of 3, co-authored 3 publications receiving 355 citations.
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Journal ArticleDOI
Emergence of Ceftazidime-Avibactam Resistance Due to Plasmid-Borne blaKPC-3 Mutations during Treatment of Carbapenem-Resistant Klebsiella pneumoniae Infections.
Ryan K. Shields,Liang Chen,Shaoji Cheng,Kalyan D. Chavda,Ellen G. Press,Avin C. Snyder,Ruchi Pandey,Yohei Doi,Barry N. Kreiswirth,M. Hong Nguyen,Cornelius J. Clancy +10 more
TL;DR: The development of resistance-conferring blaKPC-3 mutations in K. pneumoniae within 10 to 19 days of ceftazidime-avibactam exposure is troubling, but clinical impact may be ameliorated if carbapenem susceptibility is restored in certain isolates.
Journal ArticleDOI
Hsp70 and Hsp90 multichaperone complexes sequentially regulate thiazide-sensitive cotransporter endoplasmic reticulum-associated degradation and biogenesis.
Bridget F. Donnelly,Patrick G. Needham,Avin C. Snyder,Ankita Roy,Shaheen Khadem,Shaheen Khadem,Jeffrey L. Brodsky,Arohan R. Subramanya,Arohan R. Subramanya +8 more
TL;DR: Hsp70 and Hsp90 comprise two functionally distinct ER quality control checkpoints that sequentially monitor NCC biogenesis, indicating that these two proteins differentially remodel the core chaperone systems to favor cotransporter degradation andBiogenesis, respectively.
Journal ArticleDOI
The Thiazide-sensitive NaCl Cotransporter Is Targeted for Chaperone-dependent Endoplasmic Reticulum-associated Degradation
Patrick G. Needham,Kasia Mikoluk,Pradeep Dhakarwal,Shaheen Khadem,Shaheen Khadem,Avin C. Snyder,Arohan R. Subramanya,Jeffrey L. Brodsky +7 more
TL;DR: This work confirmed that NCC was a bona fide ERAD substrate in yeast, as the majority of NCC polypeptide was integrated into ER membranes, and its turnover rate was sensitive to proteasome inhibition.